SitesBLAST
Comparing WP_089301521.1 NCBI__GCF_900188115.1:WP_089301521.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P9WQ73 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
66% identity, 98% coverage: 7:373/375 of query aligns to 9:375/376 of P9WQ73
- T154 (= T152) binding
- D176 (= D174) binding
- Q199 (= Q197) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2fyfA Structure of a putative phosphoserine aminotransferase from mycobacterium tuberculosis (see paper)
66% identity, 98% coverage: 7:373/375 of query aligns to 2:367/368 of 2fyfA
- active site: F101 (= F106), D168 (= D174), K192 (= K198)
- binding tetrachloroplatinate(ii): L2 (= L7), I321 (≠ T327), A324 (= A330)
- binding pyridoxal-5'-phosphate: A77 (≠ T82), T78 (= T83), W81 (= W86), F101 (= F106), T147 (= T152), D168 (= D174), T170 (= T176), Q191 (= Q197), K192 (= K198), N243 (= N249), T244 (= T250)
Sites not aligning to the query:
3ffrA Crystal structure of a phosphoserine aminotransferase serc (chu_0995) from cytophaga hutchinsonii atcc 33406 at 1.75 a resolution
26% identity, 93% coverage: 20:367/375 of query aligns to 7:356/361 of 3ffrA
5yb0B Crystal structure of wild type phosphoserine aminotransferase (psat) from e. Histolytica (see paper)
23% identity, 93% coverage: 20:367/375 of query aligns to 4:344/349 of 5yb0B
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
24% identity, 92% coverage: 19:363/375 of query aligns to 9:357/370 of Q9Y617
- S43 (= S46) to R: in PSATD; reduced O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; 3-fold increase of KM for 3-phosphohydroxypyruvate; 5-fold increase of KM for L-glutamate; decreased function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; does not affect secondary structure; does not affect dimerization; does not affect thermal stability
- H44 (= H47) binding in other chain
- R45 (= R48) binding in other chain
- Y70 (= Y73) to N: in NLS2; uncertain significance
- G79 (≠ T82) binding ; to W: in NLS2; loss of O-phospho-L-serine:2-oxoglutarate aminotransferase activity; loss of function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway
- C80 (≠ T83) binding
- P87 (≠ A90) to A: has no effect on O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; does not affect KM for 3-phosphohydroxypyruvate; does not affect KM for L-glutamate; no effect on function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; does not affect secondary structure; does not affect dimerization; does not affect thermal stability; dbSNP:rs11540974
- A99 (≠ F101) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (≠ T102) to A: in PSATD; has no effect on O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; does not affect KM for 3-phosphohydroxypyruvate; does not affect KM for L-glutamate; does not affect secondary structure; results in increased protein aggregation as shown by dynamic light scattering; dbSNP:rs118203967
- W107 (≠ K109) binding
- E155 (= E151) to Q: in NLS2; uncertain significance
- T156 (= T152) binding
- D176 (= D174) binding
- S179 (= S177) to L: in NLS2; loss of O-phospho-L-serine:2-oxoglutarate aminotransferase activity; loss of function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; dbSNP:rs587777777
- Q199 (= Q197) binding
- K200 (= K198) modified: N6-(pyridoxal phosphate)lysine
- N241 (= N249) binding in other chain
- T242 (= T250) binding in other chain
- C245 (≠ V253) to R: in NLS2; reduced O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; 9-fold increase of KM for L-glutamate; does not affect KM for 3-phosphohydroxypyruvate; decreased function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; does not affect secondary structure; does not affect dimerization
- H335 (≠ Y339) binding
- R336 (= R340) binding
- R342 (= R348) binding ; to W: in NLS2; loss of O-phospho-L-serine:2-oxoglutarate aminotransferase activity; loss of function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; dbSNP:rs202103028
8a5vE Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
24% identity, 92% coverage: 19:363/375 of query aligns to 5:353/366 of 8a5vE
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
24% identity, 92% coverage: 19:363/375 of query aligns to 4:352/365 of 8a5wC
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
24% identity, 92% coverage: 19:363/375 of query aligns to 4:352/365 of 8a5wA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G73 (= G81), G74 (≠ T82), C75 (≠ T83), W102 (≠ K109), T151 (= T152), D171 (= D174), S173 (≠ T176), Q194 (= Q197), K195 (= K198)
- binding phosphoserine: H39 (= H47), R40 (= R48), H330 (≠ Y339), R337 (= R348)
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
24% identity, 92% coverage: 19:363/375 of query aligns to 4:352/365 of 8a5vA
8a5wE Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
24% identity, 92% coverage: 19:363/375 of query aligns to 5:352/365 of 8a5wE
- binding (2S)-2-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3-phosphonooxy-propanoic acid: H40 (= H47), R41 (= R48), N236 (= N249), T237 (= T250)
- binding (2~{S})-2-[[(~{R})-[[(5~{S})-5-azanyl-6-oxidanylidene-hexyl]amino]-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methyl]amino]-3-phosphonooxy-propanoic acid: G74 (= G81), G75 (≠ T82), C76 (≠ T83), W103 (≠ K109), T152 (= T152), S174 (≠ T176), A194 (≠ P196), Q195 (= Q197), N196 (≠ K198), H330 (≠ Y339), R331 (= R340), R337 (= R348), Y341 (≠ F352)
3e77A Human phosphoserine aminotransferase in complex with plp
23% identity, 87% coverage: 39:363/375 of query aligns to 29:350/363 of 3e77A
- active site: W100 (≠ K109), D169 (= D174), K193 (= K198)
- binding pyridoxal-5'-phosphate: G71 (= G81), G72 (≠ T82), C73 (≠ T83), W100 (≠ K109), T149 (= T152), D169 (= D174), S171 (≠ T176), Q192 (= Q197), K193 (= K198), N234 (= N249), T235 (= T250)
6czzA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with plp- phosphoserine geminal diamine intermediate (see paper)
27% identity, 68% coverage: 39:294/375 of query aligns to 32:281/360 of 6czzA
- binding pyridoxal-5'-phosphate: G74 (= G81), A75 (≠ T82), T76 (= T83), W101 (≠ F106), T151 (= T152), D171 (= D174), S173 (≠ T176), Q194 (= Q197), K195 (= K198), N236 (= N249), T237 (= T250)
- binding phosphoserine: W101 (≠ F106), T151 (= T152), K195 (= K198)
Sites not aligning to the query:
Q96255 Phosphoserine aminotransferase 1, chloroplastic; AtPSAT1; Phosphohydroxythreonine aminotransferase; EC 2.6.1.52 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 68% coverage: 39:294/375 of query aligns to 102:351/430 of Q96255
- AT 145:146 (≠ TT 82:83) binding
- W171 (≠ F106) binding
- T221 (= T152) binding
- D241 (= D174) binding
- Q264 (= Q197) binding
- K265 (= K198) modified: N6-(pyridoxal phosphate)lysine
- NT 306:307 (= NT 249:250) binding
6czyA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with pyridoxamine-5'- phosphate (pmp) (see paper)
27% identity, 68% coverage: 39:294/375 of query aligns to 34:283/362 of 6czyA
4azjA Structural basis of l-phosphoserine binding to bacillus alcalophilus phosphoserine aminotransferase (see paper)
21% identity, 92% coverage: 19:363/375 of query aligns to 6:349/360 of 4azjA
- active site: W102 (≠ K109), D172 (= D174), K196 (= K198)
- binding pyridoxal-5'-phosphate: A76 (≠ T82), S77 (≠ T83), W102 (≠ K109), T152 (vs. gap), D172 (= D174), S174 (≠ T176), Q195 (= Q197), K196 (= K198), N237 (= N249), T238 (= T250)
- binding phosphoserine: H41 (= H47), R42 (= R48), W102 (≠ K109), T152 (vs. gap), K196 (= K198), H327 (≠ Y339), R328 (= R340), R334 (= R348)
1w23B Crystal structure of phosphoserine aminotransferase from bacillus alcalophilus (see paper)
21% identity, 92% coverage: 19:363/375 of query aligns to 6:346/357 of 1w23B
- active site: W102 (≠ K109), D172 (= D174), K196 (= K198)
- binding magnesium ion: Y127 (= Y138), Y154 (vs. gap), H285 (≠ E302), A286 (≠ P303)
- binding pyridoxal-5'-phosphate: A76 (≠ T82), S77 (≠ T83), W102 (≠ K109), T152 (vs. gap), D172 (= D174), S174 (≠ T176), Q195 (= Q197), K196 (= K198), N234 (= N249), T235 (= T250)
3qboB Crystal structure of phosphoserine aminotransferase from yersinia pestis co92
25% identity, 69% coverage: 39:295/375 of query aligns to 31:282/359 of 3qboB
1bt4A Phosphoserine aminotransferase from bacillus circulans subsp. Alkalophilus
23% identity, 88% coverage: 39:368/375 of query aligns to 33:354/361 of 1bt4A
7t7jB Crystal structure of phosphoserine aminotransferase from klebsiella pneumoniae subsp. Pneumoniae in complex with pyridoxal phosphate
23% identity, 92% coverage: 19:363/375 of query aligns to 4:348/360 of 7t7jB
- binding pyridoxal-5'-phosphate: G73 (= G81), G74 (≠ T82), R75 (≠ T83), W100 (≠ F106), T151 (= T152), D172 (= D174), S174 (≠ T176), Q195 (= Q197), K196 (= K198), N237 (= N249), T238 (= T250)
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
22% identity, 96% coverage: 13:371/375 of query aligns to 13:372/381 of 2dr1A
Query Sequence
>WP_089301521.1 NCBI__GCF_900188115.1:WP_089301521.1
MTDAADLTLPDDIKPADGRFGCGPSKVRTEQLAHLASGGAAVMGTSHRQKPVKDLVGRVR
TGLRDLFNLPDGYEVLLGNGGTTAFWDAAAFGLVRERAQLFTYGEFSSKFAKVAEGAPFL
SDPIVVASEPGTAPEITYQPGADIVGWAHNETSTGVAVPVRRPAGSEGALVTIDATSGAG
GLPVAAEDFDVYYFAPQKCFAADGGLWVALASPAAVERIEEIGNSGRWVPEFLSLTTALD
NSRKNQTYNTPAVGTLLLLADQIEWMLEGGGLEWTTKRTAESARRLYEWAEKTSYTSPYV
SEPELRSHVVGTVDFADDVDATQLAATLRANGIVDVEPYRKLGRNQLRVGMFPAIEPDDI
SALIQSVDWIVERTS
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory